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Lookup NU author(s): Lorand Szabo,
Emeritus Professor Harry Gilbert
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Plant cell wall hydrolases generally have a modular structure consisting of a catalytic domain linked to one or more noncatalytic carbohydrate-binding modules (CBMs), whose common function is to attach the enzyme to the polymeric substrate. Xylanase A from Pseudomonas fluorescens subsp. cellulosa (Pf Xyn10A) consists of a family 10 catalytic domain, an N-terminal family IIa cellulose-binding module, and an internal family 10 cellulose-binding module. The structure of the 45-residue family 10 CBM has been determined in solution using NMR. It consists of two antiparallel β-sheets, one with two strands and one with three, with a short α-helix across one face of the three-stranded sheet. There is a high density of aromatic residues on one side of the protein, including three aromatic residues (Tyr8, Trp22, and Trp24), which are exposed and form a flat surface on one face, in a classical polysaccharide-binding arrangement. The fold is closely similar to that of the oligonucleotide/oligosaccharide-binding (OB) fold, but appears to have arisen by convergent evolution, because there is no sequence similarity, and the presumed binding sites are on different faces.
Author(s): Raghothama S, Simpson PJ, Szabo L, Nagy T, Gilbert HJ, Williamson MP
Publication type: Article
Publication status: Published
ISSN (print): 0006-2960
ISSN (electronic): 1520-4995
Publisher: American Chemical Society
PubMed id: 10653641
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